The structural changes of a bovine casein micelle during temperature change; in situ observation over a wide spatial scale from nano to micrometer

小角X射线散射 胶束 酪蛋白 材料科学 化学工程 化学 化学物理 分析化学(期刊) 结晶学 散射 色谱法 光学 水溶液 物理化学 有机化学 物理 工程类
作者
Hideaki Takagi,T. Nakano,Takayoshi Aoki,Morimasa Tanimoto
出处
期刊:Soft Matter [Royal Society of Chemistry]
卷期号:19 (24): 4562-4570 被引量:7
标识
DOI:10.1039/d3sm00146f
摘要

Bovine milk is the complex colloidal system containing nano to micrometer scale components. Earlier, our research group reported the structural changes in bovine casein micelles in the temperature range of 10-40 °C by in situ small-angle X-ray scattering (SAXS) [H. Takagi, T. Nakano, T. Aoki and M. Tanimoto, Food Chem., 2022, 393, 133389]. In this study, we extend our previous research by investigating the temperature-associated structural alterations in casein micelles over a wide spatial scale using in situ SAXS and ultra-SAXS (USAXS). Furthermore, the temperature dependences of various physical properties of the casein micelles were investigated by analyzing the SAXS intensities. The USAXS results showed that micelles formed 1-dimensional aggregates and that these aggregate structures did not change in the temperature range of 10-40 °C. Changes in electron densities calculated from SAXS intensities showed that the voluminosity reduced and the weight fraction of protein inside the micelles increased during the heating process. The number of water domains in a micelle decreased when the temperature increased from 10 to 40 °C, but did not substantially change in the cooling run at a rate of 1 °C min-1. The number of colloidal calcium phosphate (NCCP) in a micelle can also be calculated from the SAXS intensities; NCCP increases upon heating. This study on the behavior of casein micelles with respect to temperature change in milk over a wide spatial scale showed that the casein micelle structure was sensitive to temperature and can change dramatically with temperature variations.
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